Q92574 (TSC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 114.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Hamartin Alternative name(s): Tuberous sclerosis 1 protein | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1164 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Seems not to be required for TSC2 GAP activity towards RHEB. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. Ref.9 Ref.10 |
| Subunit structure | Interacts with TSC2, leading to stabilize TSC2. In the absence of TSC2, TSC1 self-aggregates. Interacts with DOCK7. Interacts with TBC1D7. Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 |
| Subcellular location | Cytoplasm. Membrane; Peripheral membrane protein. Note: At steady state found in association with membranes. Ref.6 |
| Tissue specificity | Highly expressed in skeletal muscle, followed by heart, brain, placenta, pancreas, lung, liver and kidney. Also expressed in embryonic kidney cells. |
| Domain | The C-terminal putative coiled-coil domain is necessary for interaction with TSC2. |
| Post-translational modification | Phosphorylation at Ser-505 does not affect interaction with TSC2. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 |
| Involvement in disease | Defects in TSC1 are the cause of tuberous sclerosis type 1 (TSC1) [MIM:191100]. It is an autosomal dominant multi-system disorder that affects especially the brain, kidneys, heart, and skin. TS1C is characterized by hamartomas (benign overgrowths predominantly of a cell or tissue type that occurs normally in the organ) and hamartias (developmental abnormalities of tissue combination). Clinical symptoms can range from benign hypopigmented macules of the skin to profound mental retardation with intractable seizures to premature death from a variety of disease-associated causes. Ref.20 Ref.22 Ref.24 Ref.25 Ref.27 Defects in TSC1 may be a cause of focal cortical dysplasia of Taylor balloon cell type (FCDBC) [MIM:607341]. FCDBC is a subtype of cortical displasias linked to chronic intractable epilepsy. Cortical dysplasias display a broad spectrum of structural changes, which appear to result from changes in proliferation, migration, differentiation, and apoptosis of neuronal precursors and neurons during cortical development. Ref.28 |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| IKBKB | O14920 | 3 | EBI-1047085,EBI-81266 | |
| MAPK14 | Q16539 | 2 | EBI-1047085,EBI-73946 | |
| NGFRAP1 | Q00994 | 5 | EBI-1047085,EBI-741753 | |
| TSC2 | P49815 | 7 | EBI-1047085,EBI-396587 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1164 | 1164 | Hamartin | PRO_0000065651 | |||||
Regions | |||||||||
| Coiled coil | 721 – 997 | 277 | Potential | ||||||
| Compositional bias | 1034 – 1037 | 4 | Poly-Gly | ||||||
| Compositional bias | 1038 – 1043 | 6 | Poly-Ser | ||||||
Amino acid modifications | |||||||||
| Modified residue | 394 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 505 | 1 | Phosphoserine Ref.11 Ref.15 Ref.16 Ref.17 Ref.18 | ||||||
| Modified residue | 511 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 598 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 1102 | 1 | Phosphoserine Ref.14 Ref.17 | ||||||
Natural variations | |||||||||
| Natural variant | 51 | 1 | E → D in TSC1; could be a polymorphism. | VAR_009397 | |||||
| Natural variant | 68 | 1 | H → R in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2. Ref.29 | VAR_054386 | |||||
| Natural variant | 72 | 1 | L → P in TSC1. Ref.22 | VAR_054387 | |||||
| Natural variant | 158 | 1 | F → C in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2. Ref.29 | VAR_054388 | |||||
| Natural variant | 190 | 1 | R → S. | VAR_009398 | |||||
| Natural variant | 191 | 1 | L → H in TSC1; could be a polymorphism. | VAR_009399 | |||||
| Natural variant | 198 – 199 | 2 | NF → I in TSC1. | VAR_009400 | |||||
| Natural variant | 206 | 1 | H → D in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2. Ref.29 | VAR_054389 | |||||
| Natural variant | 216 | 1 | F → L in a bladder tumor; diffuse punctate cytoplasmic distribution in aminoacid-starved conditions; does not affect interaction with TSC2. Ref.29 | VAR_054390 | |||||
| Natural variant | 224 | 1 | M → R in TSC1; could be a polymorphism. | VAR_009401 | |||||
| Natural variant | 322 | 1 | M → T. Ref.20 Ref.21 Ref.23 Ref.24 Ref.26 Corresponds to variant rs1073123 [ dbSNP | Ensembl ]. | VAR_009402 | |||||
| Natural variant | 417 | 1 | T → I in TSC1; could be a polymorphism; does not affect interaction with TSC2. Ref.24 Ref.26 Ref.29 | VAR_009403 | |||||
| Natural variant | 500 | 1 | R → Q in TSC1. Ref.27 | VAR_054391 | |||||
| Natural variant | 577 | 1 | E → D. Ref.26 | VAR_009404 | |||||
| Natural variant | 586 – 589 | 4 | CKIP → S in TSC1. | VAR_009405 | |||||
| Natural variant | 587 | 1 | K → R. Ref.1 Ref.21 | VAR_009406 | |||||
| Natural variant | 654 | 1 | Q → E in TSC1. Ref.24 | VAR_009407 | |||||
| Natural variant | 726 | 1 | A → E in TSC1. Ref.20 | VAR_009408 | |||||
| Natural variant | 732 | 1 | H → Y in FCDBC; could be a polymorphism. Ref.20 Ref.21 Ref.23 Ref.28 | VAR_009409 | |||||
| Natural variant | 809 | 1 | E → Q. Ref.23 | VAR_009410 | |||||
| Natural variant | 829 | 1 | S → R. Ref.26 | VAR_009411 | |||||
| Natural variant | 899 | 1 | T → S in TSC1. Ref.24 | VAR_009412 | |||||
| Natural variant | 1035 | 1 | G → S. Ref.20 Ref.21 | VAR_009413 | |||||
| Natural variant | 1108 | 1 | G → S. Ref.21 | VAR_009414 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of the tuberous sclerosis gene TSC1 on chromosome 9q34." van Slegtenhorst M.A., de Hoogt R., Hermans C., Nellist M., Janssen B., Verhoef S., Lindhout D., van den Ouweland A.M.W., Halley D.J.J., Young J., Burley M., Jeremiah S., Woodward K., Nahmias J., Fox M., Ekong R., Osborne J., Wolfe J. Kwiatkowski D.J.Science 277:805-808(1997) [PubMed: 9242607] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-587. |
| [2] | "DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. Dunham I.Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain." Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N. DNA Res. 3:321-329(1996) [PubMed: 9039502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-1164. Tissue: Bone marrow. |
| [5] | "A silent mutation 1947 T-->C in exon 15 of TSC1 in Chinese." Fang L., Wang N., Murong S.X., Wu Z.Y., Lin M.T. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 568-586. |
| [6] | "Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles." Plank T.L., Yeung R.S., Henske E.P. Cancer Res. 58:4766-4770(1998) [PubMed: 9809973] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TSC2. |
| [7] | "Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products." van Slegtenhorst M.A., Nellist M., Nagelkerken B., Cheadle J.P., Snell R.G., van den Ouweland A.M.W., Reuser A., Sampson J.R., Halley D.J.J., van der Sluijs P. Hum. Mol. Genet. 7:1053-1057(1998) [PubMed: 9580671] [Abstract] Cited for: INTERACTION WITH TSC2. |
| [8] | "Characterization of the cytosolic tuberin-hamartin complex. Tuberin is a cytosolic chaperone for hamartin." Nellist M., van Slegtenhorst M.A., Goedbloed M., van den Ouweland A.M.W., Halley D.J.J., van der Sluijs P. J. Biol. Chem. 274:35647-35652(1999) [PubMed: 10585443] [Abstract] Cited for: INTERACTION WITH TSC2. |
| [9] | "Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling." Tee A.R., Fingar D.C., Manning B.D., Kwiatkowski D.J., Cantley L.C., Blenis J. Proc. Natl. Acad. Sci. U.S.A. 99:13571-13576(2002) [PubMed: 12271141] [Abstract] Cited for: FUNCTION. |
| [10] | "Biochemical and functional characterizations of small GTPase Rheb and TSC2 GAP activity." Li Y., Inoki K., Guan K.-L. Mol. Cell. Biol. 24:7965-7975(2004) [PubMed: 15340059] [Abstract] Cited for: FUNCTION. |
| [11] | "Phosphorylation and binding partner analysis of the TSC1-TSC2 complex." Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M. Biochem. Biophys. Res. Commun. 333:818-826(2005) [PubMed: 15963462] [Abstract] Cited for: PHOSPHORYLATION AT SER-505, MASS SPECTROMETRY, INTERACTION WITH DOCK7 AND TSC2. |
| [12] | "TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase." Chong-Kopera H., Inoki K., Li Y., Zhu T., Garcia-Gonzalo F.R., Rosa J.L., Guan K.-L. J. Biol. Chem. 281:8313-8316(2006) [PubMed: 16464865] [Abstract] Cited for: INTERACTION WITH TSC2. |
| [13] | "Identification of TBC7 having TBC domain as a novel binding protein to TSC1-TSC2 complex." Nakashima A., Yoshino K., Miyamoto T., Eguchi S., Oshiro N., Kikkawa U., Yonezawa K. Biochem. Biophys. Res. Commun. 361:218-223(2007) [PubMed: 17658474] [Abstract] Cited for: INTERACTION WITH TBC1D7. |
| [14] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [15] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, MASS SPECTROMETRY. Tissue: Platelet. |
| [16] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-511 AND SER-598, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-1102, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [18] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [19] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [20] | "Molecular genetic and phenotypic analysis reveals differences between TSC1 and TSC2 associated familial and sporadic tuberous sclerosis." Jones A.C., Daniells C.E., Snell R.G., Tachataki M., Idziaszczyk S.A., Krawczak M., Sampson J.R., Cheadle J.P. Hum. Mol. Genet. 6:2155-2161(1997) [PubMed: 9328481] [Abstract] Cited for: VARIANT TSC1 GLU-726, VARIANTS THR-322; TYR-732 AND SER-1035. Tissue: Peripheral blood. |
| [21] | "Comprehensive mutational analysis of the TSC1 gene: observations on frequency of mutation, associated features, and nonpenetrance." Kwiatkowska J., Jozwiak S., Hall F., Henske E.P., Haines J.L., McNamara P., Braiser J., Wigowska-Sowinska J., Kasprzyk-Obara J., Short M.P., Kwiatkowski D.J. Ann. Hum. Genet. 62:277-285(1998) [PubMed: 9924605] [Abstract] Cited for: VARIANTS THR-322; ARG-587; TYR-732; SER-1035 AND SER-1108. Tissue: Blood. |
| [22] | "Protein truncation test for screening hamartin gene mutations and report of new disease-causing mutations." Benit P., Kara-Mostefa A., Hadj-Rabia S., Munnich A., Bonnefont J.-P. Hum. Mutat. 14:428-432(1999) [PubMed: 10533069] [Abstract] Cited for: VARIANT TSC1 PRO-72. |
| [23] | "Analysis of both TSC1 and TSC2 for germline mutations in 126 unrelated patients with tuberous sclerosis." Niida Y., Lawrence-Smith N., Banwell A., Hammer E., Lewis J., Beauchamp R.L., Sims K., Ramesh V., Ozelius L. Hum. Mutat. 14:412-422(1999) [PubMed: 10533067] [Abstract] Cited for: VARIANTS THR-322; TYR-732 AND GLN-809. Tissue: Blood and Lymphoblast. |
| [24] | "Mutational analysis of TSC1 and TSC2 genes in Japanese patients with tuberous sclerosis complex." Zhang H., Nanba E., Yamamoto T., Ninomiya H., Ohno K., Mizuguchi M., Takeshita K. J. Hum. Genet. 44:391-396(1999) [PubMed: 10570911] [Abstract] Cited for: VARIANTS TSC1 ILE-417; GLU-654 AND SER-899, VARIANT THR-322. Tissue: Blood. |
| [25] | "Mutational spectrum of the TSC1 gene in a cohort of 225 tuberous sclerosis complex patients: no evidence for genotype-phenotype correlation." Van Slegtenhorst M.A., Verhoef S., Tempelaars A., Bakker L., Wang Q., Wessels M., Bakker R., Nellist M., Lindhout D., Halley D.J.J., van den Ouweland A.M.W. J. Med. Genet. 36:285-289(1999) [PubMed: 10227394] [Abstract] Cited for: VARIANTS TSC1, VARIANTS. Tissue: Peripheral blood. |
| [26] | "Analysis of all exons of TSC1 and TSC2 genes for germline mutations in Japanese patients with tuberous sclerosis: report of 10 mutations." Yamashita Y., Ono J., Okada S., Wataya-Kaneda M., Yoshikawa K., Nishizawa M., Hirayama Y., Kobayashi E., Seyama K., Hino O. Am. J. Med. Genet. 90:123-126(2000) [PubMed: 10607950] [Abstract] Cited for: VARIANTS THR-322; ILE-417; ASP-577 AND ARG-829. Tissue: Peripheral blood leukocyte. |
| [27] | "Tuberous sclerosis type 1: three novel mutations detected in exon 15 by a combination of HDA and TGGE." Hass J., Mayer K., Rott H.-D. Hum. Mutat. 16:88-88(2000) [PubMed: 10874311] [Abstract] Cited for: VARIANT TSC1 GLN-500. |
| [28] | "Focal cortical dysplasia of Taylor's balloon cell type: mutational analysis of the TSC1 gene indicates a pathogenic relationship to tuberous sclerosis." Becker A.J., Urbach H., Scheffler B., Baden T., Normann S., Lahl R., Pannek H.W., Tuxhorn I., Elger C.E., Schramm J., Wiestler O.D., Bluemcke I. Ann. Neurol. 52:29-37(2002) [PubMed: 12112044] [Abstract] Cited for: VARIANT FCDBC TYR-732. |
| [29] | "Bladder tumour-derived somatic TSC1 missense mutations cause loss of function via distinct mechanisms." Pymar L.S., Platt F.M., Askham J.M., Morrison E.E., Knowles M.A. Hum. Mol. Genet. 17:2006-2017(2008) [PubMed: 18397877] [Abstract] Cited for: VARIANTS ARG-68; CYS-158; ASP-206; LEU-216 AND ILE-417, CHARACTERIZATION OF VARIANTS ARG-68; CYS-158; ASP-206; LEU-216 AND ILE-417. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF013168 mRNA. Translation: AAC51674.1. AL445645 Genomic DNA. Translation: CAH72112.1. CH471090 Genomic DNA. Translation: EAW88021.1. AC002096 Genomic DNA. No translation available. D87683 mRNA. Translation: BAA13436.1. AF234185 Genomic DNA. Translation: AAF61948.1. |
| IPI | IPI00022043. |
| PIR | T03814. |
| RefSeq | NP_000359.1. NM_000368.4. NP_001155898.1. NM_001162426.1. NP_001155899.1. NM_001162427.1. |
| UniGene | Hs.370854. |
3D structure databases | |
| ProteinModelPortal | Q92574. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q92574. 32 interactions. |
| MINT | MINT-1534928. |
| STRING | Q92574. |
PTM databases | |
| PhosphoSite | Q92574. |
Polymorphism databases | |
| DMDM | 9297077. |
Proteomic databases | |
| PRIDE | Q92574. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000298552; ENSP00000298552; ENSG00000165699. ENST00000440111; ENSP00000394524; ENSG00000165699. |
| GeneID | 7248. |
| KEGG | hsa:7248. |
| UCSC | uc004cca.1. human. |
Organism-specific databases | |
| CTD | 7248. |
| GeneCards | GC09M135766. |
| H-InvDB | HIX0008496. |
| HGNC | HGNC:12362. TSC1. |
| HPA | CAB011568. CAB012481. |
| MIM | 191100. phenotype. 605284. gene. 607341. phenotype. |
| neXtProt | NX_Q92574. |
| Orphanet | 65683. Isolated focal cortical dysplasia. 538. Lymphangioleiomyomatosis. 805. Tuberous sclerosis. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| GeneTree | ENSGT00390000014148. |
| HOGENOM | HBG445246. |
| HOVERGEN | HBG012559. |
| InParanoid | Q92574. |
| OMA | GFDSPFY. |
| OrthoDB | EOG4S4PFD. |
| PhylomeDB | Q92574. |
Enzyme and pathway databases | |
| Pathway_Interaction_DB | pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. mtor_4pathway. mTOR signaling pathway. |
| Reactome | REACT_111102. Signal Transduction. |
Gene expression databases | |
| ArrayExpress | Q92574. |
| Bgee | Q92574. |
| CleanEx | HS_TSC1. |
| Genevestigator | Q92574. |
| GermOnline | ENSG00000165699. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR007483. Hamartin. [Graphical view] |
| KO | K07206. |
| PANTHER | PTHR15154. Hamartin. 1 hit. |
| Pfam | PF04388. Hamartin. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 28341. |
| SOURCE | Search... |
Entry information
| Entry name | TSC1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q92574 Secondary accession number(s): Q5VVN5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 9 Human chromosome 9: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |

Clusters with